Link to this page
Human Interaction Network Ontology
Last uploaded:
June 27, 2014
Jump to:
| Id | http://purl.obolibrary.org/obo/HINO_0007908
http://purl.obolibrary.org/obo/HINO_0007908
|
|---|---|
| Preferred Name | Interaction of PIN1 with p-IRF3 |
| Definitions |
Reviewed: Kawai, T, Akira, S, 2010-10-30
Edited: Garapati, P V, 2010-08-02
Two cluster of serine residues in the C-terminus of IRF3 are essential for its activation. Cluster 1, comprising Ser385 and Ser386, is essential for the formation of IRF3 dimers. The second cluster include a series of serine and threonine residues between Ser396 and Ser405. Phosphorylation of residues in both clusters has been noted in response to virus infection and dsRNA treatment, and the IKKi/TBK1 kinase complex has been shown to phosphorylate both clusters. <br>Yamaoka et al has shown that IRF3 is also phosphorylated on Ser339 after dsRNA stimulation, however this phosphorylation is associated with destabilization rather than activation of IRF3. This Ser339 precedes a proline residue 340 (Pro340) and this serine-proline motif acts as a binding site for the protein PIN1, a peptidyl-prolyl-isomerase. PIN1 consist of two distinct domains, a short N-terminal WW domain and a C-terminal catalytic domain. The WW domain of PIN1 is involved in binding the ser339-pro340 region. Yamaoka et al showed that exogenous expression of PIN1 suppresses IRF3 activation and type I interferon production and, conversely, that siRNA silencing of PIN1 leads to enhancement of IRF3 activation and IFNB production.
Authored: Garapati, P V, 2010-08-02
|
| Type | http://www.w3.org/2002/07/owl#Class |
All Properties
| label |
Interaction of PIN1 with p-IRF3
|
|---|---|
| comment |
Reviewed: Kawai, T, Akira, S, 2010-10-30
Edited: Garapati, P V, 2010-08-02
Two cluster of serine residues in the C-terminus of IRF3 are essential for its activation. Cluster 1, comprising Ser385 and Ser386, is essential for the formation of IRF3 dimers. The second cluster include a series of serine and threonine residues between Ser396 and Ser405. Phosphorylation of residues in both clusters has been noted in response to virus infection and dsRNA treatment, and the IKKi/TBK1 kinase complex has been shown to phosphorylate both clusters. <br>Yamaoka et al has shown that IRF3 is also phosphorylated on Ser339 after dsRNA stimulation, however this phosphorylation is associated with destabilization rather than activation of IRF3. This Ser339 precedes a proline residue 340 (Pro340) and this serine-proline motif acts as a binding site for the protein PIN1, a peptidyl-prolyl-isomerase. PIN1 consist of two distinct domains, a short N-terminal WW domain and a C-terminal catalytic domain. The WW domain of PIN1 is involved in binding the ser339-pro340 region. Yamaoka et al showed that exogenous expression of PIN1 suppresses IRF3 activation and type I interferon production and, conversely, that siRNA silencing of PIN1 leads to enhancement of IRF3 activation and IFNB production.
Authored: Garapati, P V, 2010-08-02
|
| prefLabel |
Interaction of PIN1 with p-IRF3
|
| definition source |
Pubmed16715065
Reactome, http://www.reactome.org
Pubmed19125153
Pubmed16699525
|
| prefixIRI |
HINO:0007908
|
| seeAlso |
Reactome Database ID Release 43936380
ReactomeREACT_25077
|
| subClassOf | |
| type | |
| has input | |
| has output |
Add comment
| Delete | Subject | Author | Type | Created |
|---|---|---|---|---|
| No notes to display |